Evidence map›Paper›PMID 33383640›Full record

ArticleMolecules (Basel, Switzerland)2020

Reversible Dimerization of Human Serum Albumin.

Alexey Chubarov, Anna Spitsyna, Olesya Krumkacheva, Dmitry Mitin, Daniil Suvorov, Victor Tormyshev, Matvey Fedin, Michael K Bowman, Elena Bagryanskaya

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.1field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Organic-solvent mediated self-assembly of protoporphyrin IX with human serum albumin.International journal of biological macromolecules · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. [Research progress on detection techniques for effective albumin concentration].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2024
    Review
  11. Article
  12. Contrast Agents Based on Human Serum Albumin and Nitroxides forInternational journal of molecular sciences · 2024
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Fluorinated Human Serum Albumin as PotentialMolecules (Basel, Switzerland) · 2023
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Alexey ChubarovInstitute of Chemical Biology and Fundamental Medicine SB RAS, 630090 Novosibirsk, Russia.ORCID 0000-0002-5708-7595
Anna SpitsynaNovosibirsk State University, 630090 Novosibirsk, Russia.
Olesya KrumkachevaNovosibirsk State University, 630090 Novosibirsk, Russia.ORCID 0000-0002-0777-5103
Dmitry MitinInstitute of Chemical Biology and Fundamental Medicine SB RAS, 630090 Novosibirsk, Russia.
Daniil SuvorovInstitute of Chemical Biology and Fundamental Medicine SB RAS, 630090 Novosibirsk, Russia.
Victor TormyshevInternational Tomography Center SB RAS, 630090 Novosibirsk, Russia.
Matvey FedinNovosibirsk State University, 630090 Novosibirsk, Russia.ORCID 0000-0002-0537-5755
Michael K BowmanInternational Tomography Center SB RAS, 630090 Novosibirsk, Russia.
Elena BagryanskayaInternational Tomography Center SB RAS, 630090 Novosibirsk, Russia.ORCID 0000-0003-0057-383X
Novosibirsk State University · RUInternational Tomography Center · RUUniversity of Alabama · US

Funding

Ministry of Science and Education of the Russian Federation 14.W03.31.0034Russian Foundation for Basic Research 18-04-00393
6 · The paper itself

Abstract

Pulsed Dipolar Spectroscopy (PDS) methods of Electron Paramagnetic Resonance (EPR) were used to detect and characterize reversible non-covalent dimers of Human Serum Albumin (HSA), the most abundant protein in human plasma. The spin labels, MTSL and OX063, were attached to Cys-34 and these chemical modifications of Cys-34 did affect the dimerization of HSA, indicating that other post-translational modifications can modulate dimer formation. At physiologically relevant concentrations, HSA does form weak, non-covalent dimers with a well-defined structure. Dimer formation is readily reversible into monomers. Dimerization is very relevant to the role of HSA in the transport, binding, and other physiological processes.

Indexed as

CysteineElectron Spin Resonance SpectroscopyHumansProtein MultimerizationSerum Albumin, HumanSpin LabelsCysteineSerum Albumin, HumanSpin Labelsaggregationhuman serum albuminpulse dipole EPR

Identifiers

PMID33383640
PMCPMC7795135
OpenAlexW3117876055

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.